Evidence map›Paper›PMID 24390573›Full record

ReviewMolecular neurobiology2014

Protein prenylation and synaptic plasticity: implications for Alzheimer's disease.

David A Hottman, Ling Li

Open access · greenAbstract readReview
In one paragraph

Review in Molecular neurobiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.7field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

36 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. ACS chemical biology · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. ACS chemical biology · 2022
    Article
  14. Review
  15. Article
  16. Article
  17. Posttranslational modifications in proteins: resources, tools and prediction methods.Database : the journal of biological databases and curation · 2021
    Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

David A HottmanDepartment of Experimental and Clinical Pharmacology, University of Minnesota, 2001 6th St SE, MTRF 4-208, Minneapolis, MN, 55455, USA.
Ling Li
University of Minnesota · US

Funding

Protective Mechanisms of Statins in Alzheimer's DiseaseR01AG031846 · NIA · UNIVERSITY OF MINNESOTA · PI LI, LING · 2008 to 2012
$1.5M
NIA NIH HHS AG031846NIA NIH HHS R01 AG031846
6 · The paper itself

Abstract

Protein prenylation is an important lipid posttranslational modification of proteins. It includes protein farnesylation and geranylgeranylation, in which the 15-carbon farnesyl pyrophosphate or 20-carbon geranylgeranyl pyrophosphate is attached to the C-terminus of target proteins, catalyzed by farnesyl transferase or geranylgeranyl transferases, respectively. Protein prenylation facilitates the anchoring of proteins into the cell membrane and mediates protein-protein interactions. Among numerous proteins that undergo prenylation, small GTPases represent the largest group of prenylated proteins. Small GTPases are involved in regulating a plethora of cellular functions including synaptic plasticity. The prenylation status of small GTPases determines the subcellular locations and functions of the proteins. Dysregulation or dysfunction of small GTPases leads to the development of different types of disorders. Emerging evidence indicates that prenylated proteins, in particular small GTPases, may play important roles in the pathogenesis of Alzheimer's disease. This review focuses on the prenylation of Ras and Rho subfamilies of small GTPases and its relation to synaptic plasticity and Alzheimer's disease.

Indexed as

Alzheimer DiseaseAnimalsHumansNeuronal PlasticityNeuronsProtein PrenylationProtein Processing, Post-Translationalras Proteinsrho GTP-Binding Proteinsras Proteinsrho GTP-Binding Proteins

Identifiers

PMID24390573
PMCPMC4082763
OpenAlexW2076495844

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.